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10.1111/febs.14707 http://scihub22266oqcxt.onion/10.1111/febs.14707 30461192!7164057!30461192     free     free     free Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       FEBS+J 2019 ; 286 (4): 765-787 Nephropedia Template TP {{tp|p=30461192|t=2019. Toward development of generic inhibitors against the 3C proteases of picornaviruses |pdf=|usr=}}{{30461192}} gab.com Text Toward development of generic inhibitors against the 3C proteases of picornaviruses JO: FEBS J http://www.kidney.de/pget.php?&tw=1&pmid=30461192 #FOAvip Development of novel antivirals, which requires knowledge of the viral life cycle in molecular detail, is a daunting task, involving extensive investments, and frequently resulting in failure. As there exist significant commonalities among virus families in the manner of host interaction, identifying and targeting common rather than specific features may lead to the development of broadly useful antivirals. Here, we have targeted the 3C protease of Hepatitis A Virus (HAV), a feco-orally transmitted virus of the family Picornaviridae, for identification of potential antivirals. The 3C protease is a viable drug target as it is required by HAV, as well as by other picornaviruses, for post-translational proteolysis of viral polyproteins and for inhibiting host innate immune pathways. Computational screening, followed by chemical synthesis and experimental validation resulted in identification of a few compounds which, at low micromolar concentrations, could inhibit HAV 3C activity. These compounds were further tested experimentally against the 3C protease of Human Rhinovirus, another member of the Picornaviridae family, with comparable results. Computational studies on 3C proteases from other members of the picornavirus family have indicated that the compounds identified could potentially be generic inhibitors for picornavirus 3C proteases. Twit Text FOAVip Toward development of generic inhibitors against the 3C proteases of picornaviruses ????FEBS J http://www.kidney.de/pget.php?&tw=1&pmid=30461192 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=30461192 #FOAvip English Wikipedia <ref>{{Cite pmid|30461192}}</ref> Toward development of generic inhibitors against the 3C proteases of picornaviruses #MMPMID30461192 Banerjee K; Bhat R; Rao VUB; Nain A; Rallapalli KL; Gangopadhyay S; Singh RP; Banerjee M; Jayaram B FEBS J 2019[Feb]; 286 (4): 765-787 PMID30461192show ga Development of novel antivirals, which requires knowledge of the viral life cycle in molecular detail, is a daunting task, involving extensive investments, and frequently resulting in failure. As there exist significant commonalities among virus families in the manner of host interaction, identifying and targeting common rather than specific features may lead to the development of broadly useful antivirals. Here, we have targeted the 3C protease of Hepatitis A Virus (HAV), a feco-orally transmitted virus of the family Picornaviridae, for identification of potential antivirals. The 3C protease is a viable drug target as it is required by HAV, as well as by other picornaviruses, for post-translational proteolysis of viral polyproteins and for inhibiting host innate immune pathways. Computational screening, followed by chemical synthesis and experimental validation resulted in identification of a few compounds which, at low micromolar concentrations, could inhibit HAV 3C activity. These compounds were further tested experimentally against the 3C protease of Human Rhinovirus, another member of the Picornaviridae family, with comparable results. Computational studies on 3C proteases from other members of the picornavirus family have indicated that the compounds identified could potentially be generic inhibitors for picornavirus 3C proteases. |*Drug Development[MESH] |3C Viral Proteases[MESH] |Antiviral Agents/*chemistry/*pharmacology[MESH] |Cysteine Endopeptidases[MESH] |Hepatitis A virus/*enzymology[MESH] |Humans[MESH] |Molecular Conformation[MESH] |Molecular Dynamics Simulation[MESH] |Protease Inhibitors/*chemistry/*pharmacology[MESH]Toward development of generic inhibitors against the 3C proteases of (epmc).pdf DeepDyve Pubget Overpricing